ID SET1_CAEEL Reviewed; 242 AA. AC Q22795; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1999, sequence version 2. DT 23-FEB-2022, entry version 143. DE RecName: Full=Histone-lysine N-methyltransferase set-1; DE EC=2.1.1.361 {ECO:0000255|PROSITE-ProRule:PRU00904, ECO:0000269|PubMed:23028348}; GN Name=set-1; ORFNames=T26A5.7; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [2] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=12119097; DOI=10.1016/s0378-1119(02)00671-6; RA Terranova R., Pujol N., Fasano L., Djabali M.; RT "Characterisation of set-1, a conserved PR/SET domain gene in RT Caenorhabditis elegans."; RL Gene 292:33-41(2002). RN [3] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22393255; DOI=10.1128/mcb.06546-11; RA Wells M.B., Snyder M.J., Custer L.M., Csankovszki G.; RT "Caenorhabditis elegans dosage compensation regulates histone H4 chromatin RT state on X chromosomes."; RL Mol. Cell. Biol. 32:1710-1719(2012). RN [4] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=23028348; DOI=10.1371/journal.pgen.1002933; RA Vielle A., Lang J., Dong Y., Ercan S., Kotwaliwale C., Rechtsteiner A., RA Appert A., Chen Q.B., Dose A., Egelhofer T., Kimura H., Stempor P., RA Dernburg A., Lieb J.D., Strome S., Ahringer J.; RT "H4K20me1 contributes to downregulation of X-linked genes for C. elegans RT dosage compensation."; RL PLoS Genet. 8:E1002933-E1002933(2012). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=23884442; DOI=10.1242/dev.094292; RA Webster C.M., Wu L., Douglas D., Soukas A.A.; RT "A non-canonical role for the C. elegans dosage compensation complex in RT growth and metabolic regulation downstream of TOR complex 2."; RL Development 140:3601-3612(2013). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=28867287; DOI=10.1016/j.cell.2017.07.041; RA Brejc K., Bian Q., Uzawa S., Wheeler B.S., Anderson E.C., King D.S., RA Kranzusch P.J., Preston C.G., Meyer B.J.; RT "Dynamic Control of X Chromosome Conformation and Repression by a Histone RT H4K20 Demethylase."; RL Cell 171:E23-E23(2017). CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates CC 'Lys-20' of histone H4 (H4K20me1) (PubMed:23028348). H4K20me1 is CC enriched on hermaphrodite X chromosomes and during mitosis CC (PubMed:23028348, PubMed:22393255). Involved in dosage compensation by CC repression of X-linked gene expression in hermaphrodites CC (PubMed:23028348). Plays a role in growth and body fat regulation CC downstream of the TOR complex 2 pathway (PubMed:23884442). CC {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348, CC ECO:0000269|PubMed:23884442}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00904, CC ECO:0000269|PubMed:23028348}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12119097}. Chromosome CC {ECO:0000305|PubMed:23028348}. CC -!- TISSUE SPECIFICITY: In embryos, it is expressed ubiquitously. In late CC embryos, it is expressed in hypodermal seam cells. In L3 and L4 larvae CC and thereafter, it is expressed in vulval precursor cells. In adult CC males, it is also expressed in 6 unidentified posterior cells. CC {ECO:0000269|PubMed:12119097}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in eggs, then decreases. CC {ECO:0000269|PubMed:12119097}. CC -!- DISRUPTION PHENOTYPE: Mutant animals lack methylation of 'Lys-20' of CC histone H4 (H4K20me) (PubMed:23028348). In a glp-1(e2141) mutant CC background which lacks a germline, the X-linked genes aco-1, ajm-1 and CC apl-1 are up-regulated (PubMed:23028348). RNAi-mediated knockdown leads CC to embryonic lethality in a mutant background of the dosage CC compensation proteins dpy-21 or dpy-28 (PubMed:23028348). Increases CC 'Lys-16' acetylation of histone H4 on hermaphrodite X chromosomes CC (PubMed:22393255). In the TOR complex 2 mutant background rict-1, CC suppresses the growth delay and elevated body fat index CC (PubMed:23884442). Causes mitotic chromosome segregation defects and CC chromosome bridges resulting in delayed or arrested embryonic CC development and embryonic lethality (PubMed:28867287). CC {ECO:0000269|PubMed:22393255, ECO:0000269|PubMed:23028348, CC ECO:0000269|PubMed:23884442, ECO:0000269|PubMed:28867287}. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. PR/SET subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00904}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FO080366; CCD63213.1; -; Genomic_DNA. DR PIR; T34384; T34384. DR RefSeq; NP_001022796.1; NM_001027625.3. DR SMR; Q22795; -. DR BioGRID; 41136; 14. DR IntAct; Q22795; 12. DR STRING; 6239.T26A5.7a; -. DR EPD; Q22795; -. DR PaxDb; Q22795; -. DR EnsemblMetazoa; T26A5.7a.1; T26A5.7a.1; WBGene00004781. DR GeneID; 175918; -. DR KEGG; cel:CELE_T26A5.7; -. DR UCSC; T26A5.7b.1; c. elegans. DR CTD; 175918; -. DR WormBase; T26A5.7a; CE19602; WBGene00004781; set-1. DR eggNOG; KOG1085; Eukaryota. DR GeneTree; ENSGT00940000163293; -. DR HOGENOM; CLU_047978_2_1_1; -. DR InParanoid; Q22795; -. DR OMA; ATKESPW; -. DR OrthoDB; 1460495at2759; -. DR PhylomeDB; Q22795; -. DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes. DR Reactome; R-CEL-3214841; PKMTs methylate histone lysines. DR PRO; PR:Q22795; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00004781; Expressed in multi-cellular organism and 7 other tissues. DR ExpressionAtlas; Q22795; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase. DR InterPro; IPR016858; Hist_H4-K20_MeTrfase. DR InterPro; IPR001214; SET_dom. DR Pfam; PF00856; SET; 1. DR PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1. DR SMART; SM00317; SET; 1. DR PROSITE; PS51571; SAM_MT43_PR_SET; 1. DR PROSITE; PS50280; SET; 1. PE 1: Evidence at protein level; KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus; KW Reference proteome; S-adenosyl-L-methionine; Transcription; KW Transcription regulation; Transferase. FT CHAIN 1..242 FT /note="Histone-lysine N-methyltransferase set-1" FT /id="PRO_0000097694" FT DOMAIN 104..226 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 114..116 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904" FT REGION 186..187 FT /note="S-adenosyl-L-methionine binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00904" FT COMPBIAS 23..54 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 159 FT /note="S-adenosyl-L-methionine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190, FT ECO:0000255|PROSITE-ProRule:PRU00904" SQ SEQUENCE 242 AA; 27568 MW; 0F752B79505AFA99 CRC64; MKVAAKKLAT SRMRKDRAAA ASPSSDIENS ENPSSLASHS SSSGRMTPSK NTRSRKGVSV KDVSNHKITE FFQVRRSNRK TSKQISDEAK HALRDTVLKG TNERLLEVYK DVVKGRGIRT KVNFEKGDFV VEYRGVMMEY SEAKVIEEQY SNDEEIGSYM YFFEHNNKKW CIDATKESPW KGRLINHSVL RPNLKTKVVE IDGSHHLILV ARRQIAQGEE LLYDYGDRSA ETIAKNPWLV NT //